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Q8DVD3 (SYI_STRMU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Isoleucine--tRNA ligase

EC=6.1.1.5
Alternative name(s):
Isoleucyl-tRNA synthetase
Short name=IleRS
Gene names
Name:ileS
Ordered Locus Names:SMU_558
OrganismStreptococcus mutans serotype c (strain ATCC 700610 / UA159) [Complete proteome] [HAMAP]
Taxonomic identifier210007 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length930 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile) By similarity. HAMAP-Rule MF_02002

Catalytic activity

ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP-Rule MF_02002

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_02002

Subunit structure

Monomer By similarity. HAMAP-Rule MF_02002

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_02002.

Domain

IleRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated valine is translocated from the active site to the editing site, which sterically excludes the correctly activated isoleucine. The single editing site contains two valyl binding pockets, one specific for each substrate (Val-AMP or Val-tRNA(Ile)) By similarity. HAMAP-Rule MF_02002

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processisoleucyl-tRNA aminoacylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

aminoacyl-tRNA editing activity

Inferred from electronic annotation. Source: InterPro

isoleucine-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 930930Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098478

Regions

Motif57 – 6711"HIGH" region HAMAP-Rule MF_02002
Motif595 – 5995"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8881Zinc By similarity
Metal binding8911Zinc By similarity
Metal binding9081Zinc By similarity
Metal binding9111Zinc By similarity
Binding site5541Aminoacyl-adenylate By similarity
Binding site5981ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8DVD3 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 40024D46A4BAE8C2

FASTA930105,853
        10         20         30         40         50         60 
MKLKETLNLG KTAFPMRAGL PNKEPQWQKQ WDEANIYAKR QELNANKPAF FLHDGPPYAN 

        70         80         90        100        110        120 
GNIHVGHALN KISKDIIIRS KSMSGFRAPY IPGWDTHGLP IEQVLAKKGV KRKEIDLADY 

       130        140        150        160        170        180 
LDMCRQYALS QVDKQRQDFK RLGVSGDWEN PYITLVPKYE AAQIRVFGAM ADKGYIYHGA 

       190        200        210        220        230        240 
KPVYWSWSSE SALAEAEIEY HDIDSTSLYY ANRVKDGKDI LDTDTYIVVW TTTPFTITAS 

       250        260        270        280        290        300 
RGLTVGPDID YVVVKPANDE RKFLVAQALL SELAERFAWD NPQVLATHKG IELDRIVTIH 

       310        320        330        340        350        360 
PWDDNVEELV MNGDHVTLDS GTGIVHTAPG FGEDDYNVGV KYGLDVVVTV NERGIMMENA 

       370        380        390        400        410        420 
GPDFEGQFYD KVLPTVKEKL GDLLLASEVI THSYPFDWRT KKPIIWRAVP QWFASVSKFR 

       430        440        450        460        470        480 
QDILDEIDKV HFYPAWGKTR LYNMIRDRGD WVISRQRAWG VPLPIFYAED GTAIMTKEVT 

       490        500        510        520        530        540 
DHIANLFEEH GSVIWWQREA KDLLPEGFTH PGSPNGEFTK ENDIMDVWFD SGSSWNGVLN 

       550        560        570        580        590        600 
TREDLGYPAD LYLEGSDQYR GWFNSSLITS VAVNGHAPYK SVLSQGFVLD GKGEKMSKSK 

       610        620        630        640        650        660 
GNIISPNDVA KQYGAEILRL WVASVDTDSD VRVSMEILGQ VSETYRKIRN TLRFLIANTT 

       670        680        690        700        710        720 
DFNPYINKIA FEDLRSVDKY MLIKFNQLVS VINRAYSHYD FMTIYKAVVN FVTVDLSAFY 

       730        740        750        760        770        780 
LDFAKDVVYI EAADDLARRQ MQTVFYEILV NITKLLTPIL PHTSEEIWSY LEHEEEAFVQ 

       790        800        810        820        830        840 
LAEMPEAQEF ANQDEILDTW SAFMSLRDQA QKALEEARNA KIIGKSLEAH LTVYASEEVK 

       850        860        870        880        890        900 
TLLTALDSNI AQLLIVSQLT VTQEQAPKNA LVFEDVAFSV EHARGHVCDR CRRIDETVKE 

       910        920        930 
RPYHVTICNH CAAIVENHFP EAVRQGFESK 

« Hide

References

[1]"Genome sequence of Streptococcus mutans UA159, a cariogenic dental pathogen."
Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B., Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S., Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.
Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700610 / UA159.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014133 Genomic DNA. Translation: AAN58300.1.
RefSeqNP_720994.1. NC_004350.2.

3D structure databases

ProteinModelPortalQ8DVD3.
SMRQ8DVD3. Positions 1-918.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING210007.SMU.558.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN58300; AAN58300; SMU_558.
GeneID1028027.
KEGGsmu:SMU_558.
PATRIC19663321. VBIStrMut61772_0493.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
KOK01870.
OMAVLGDWDN.
OrthoDBEOG644ZM1.
ProtClustDBPRK05743.

Enzyme and pathway databases

BioCycSMUT210007:GC7Z-550-MONOMER.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPMF_02002. Ile_tRNA_synth_type1.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR002301. Ile-tRNA-ligase.
IPR023585. Ile-tRNA-ligase_type1.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
IPR013155. V/L/I-tRNA-synth_anticodon-bd.
IPR009008. Val/Leu/Ile-tRNA-synth_edit.
IPR010663. Znf_DNA_glyclase/IsotRNA_synth.
[Graphical view]
PANTHERPTHR11946:SF9. PTHR11946:SF9. 1 hit.
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
PF06827. zf-FPG_IleRS. 1 hit.
[Graphical view]
PRINTSPR00984. TRNASYNTHILE.
SUPFAMSSF47323. SSF47323. 1 hit.
SSF50677. SSF50677. 1 hit.
TIGRFAMsTIGR00392. ileS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYI_STRMU
AccessionPrimary (citable) accession number: Q8DVD3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: March 1, 2003
Last modified: April 16, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries